Biomechanical origins of inherent tension in fibrin networks.
Blood clotting
Fiber relaxation
Fibrin networks
Helical fibers
Inherent tension
Journal
Journal of the mechanical behavior of biomedical materials
ISSN: 1878-0180
Titre abrégé: J Mech Behav Biomed Mater
Pays: Netherlands
ID NLM: 101322406
Informations de publication
Date de publication:
09 2022
09 2022
Historique:
received:
28
04
2022
revised:
02
06
2022
accepted:
18
06
2022
pubmed:
9
7
2022
medline:
22
7
2022
entrez:
8
7
2022
Statut:
ppublish
Résumé
Blood clots form at the site of vascular injury to seal the wound and prevent bleeding. Clots are in tension as they perform their biological functions and withstand hydrodynamic forces of blood flow, vessel wall fluctuations, extravascular muscle contraction and other forces. There are several mechanisms that generate tension in a blood clot, of which the most well-known is the contraction/retraction caused by activated platelets. Here we show through experiments and modeling that clot tension is generated by the polymerization of fibrin. Our mathematical model is built on the hypothesis that the shape of fibrin monomers having two-fold symmetry and off-axis binding sites is ultimately the source of inherent tension in individual fibers and the clot. As the diameter of a fiber grows during polymerization the fibrin monomers must suffer axial twisting deformation so that they remain in register to form the half-staggered arrangement characteristic of fibrin protofibrils. This deformation results in a pre-strain that causes fiber and network tension. Our results for the pre-strain in single fibrin fibers is in agreement with experiments that measured it by cutting fibers and measuring their relaxed length. We connect the mechanics of a fiber to that of the network using the 8-chain model of polymer elasticity. By combining this with a continuum model of swellable elastomers we can compute the evolution of tension in a constrained fibrin gel. The temporal evolution and tensile stresses predicted by this model are in qualitative agreement with experimental measurements of the inherent tension of fibrin clots polymerized between two fixed rheometer plates. These experiments also revealed that increasing thrombin concentration leads to increasing internal tension in the fibrin network. Our model may be extended to account for other mechanisms that generate pre-strains in individual fibers and cause tension in three-dimensional proteinaceous polymeric networks.
Identifiants
pubmed: 35803206
pii: S1751-6161(22)00240-5
doi: 10.1016/j.jmbbm.2022.105328
pmc: PMC9434494
mid: NIHMS1832025
pii:
doi:
Substances chimiques
Fibrin
9001-31-4
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
105328Subventions
Organisme : NHLBI NIH HHS
ID : R00 HL148646
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL135254
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL148227
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM135141
Pays : United States
Informations de copyright
Copyright © 2022 Elsevier Ltd. All rights reserved.
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